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Database: UniProt
Entry: A4ITM1_GEOTN
LinkDB: A4ITM1_GEOTN
Original site: A4ITM1_GEOTN 
ID   A4ITM1_GEOTN            Unreviewed;      1086 AA.
AC   A4ITM1;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=Fused isobutyryl-CoA mutase {ECO:0000256|HAMAP-Rule:MF_02050};
DE   Includes:
DE     RecName: Full=Isobutyryl-CoA mutase {ECO:0000256|HAMAP-Rule:MF_02050};
DE              Short=ICM {ECO:0000256|HAMAP-Rule:MF_02050};
DE              EC=5.4.99.13 {ECO:0000256|HAMAP-Rule:MF_02050};
DE   Includes:
DE     RecName: Full=P-loop GTPase {ECO:0000256|HAMAP-Rule:MF_02050};
DE              EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_02050};
DE     AltName: Full=G-protein chaperone {ECO:0000256|HAMAP-Rule:MF_02050};
GN   Name=icmF {ECO:0000256|HAMAP-Rule:MF_02050};
GN   OrderedLocusNames=GTNG_3336 {ECO:0000313|EMBL:ABO68675.1};
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO68675.1, ECO:0000313|Proteomes:UP000001578};
RN   [1] {ECO:0000313|EMBL:ABO68675.1, ECO:0000313|Proteomes:UP000001578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2 {ECO:0000313|EMBL:ABO68675.1,
RC   ECO:0000313|Proteomes:UP000001578};
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of isobutyryl-CoA
CC       and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase
CC       activity, associated with its G-protein domain (MeaI) that functions as
CC       a chaperone that assists cofactor delivery and proper holo-enzyme
CC       assembly. {ECO:0000256|HAMAP-Rule:MF_02050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylpropanoyl-CoA = butanoyl-CoA; Xref=Rhea:RHEA:13141,
CC         ChEBI:CHEBI:57338, ChEBI:CHEBI:57371; EC=5.4.99.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02050};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02050};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02050};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922,
CC         ECO:0000256|HAMAP-Rule:MF_02050};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02050}.
CC   -!- DOMAIN: Is composed of four functional domains: the N-terminal 5'-
CC       deoxyadenosylcobalamin binding region that is homologous to the small
CC       subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely
CC       acts as a chaperone for ICM, a structured linker region involved in
CC       dimer formation, and a C-terminal part that is homologous to the large
CC       substrate-binding subunit of ICM (IcmA). {ECO:0000256|HAMAP-
CC       Rule:MF_02050}.
CC   -!- SIMILARITY: Belongs to the IcmF family. {ECO:0000256|HAMAP-
CC       Rule:MF_02050}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02050}.
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DR   EMBL; CP000557; ABO68675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4ITM1; -.
DR   KEGG; gtn:GTNG_3336; -.
DR   eggNOG; COG1703; Bacteria.
DR   eggNOG; COG1884; Bacteria.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_009523_2_0_9; -.
DR   OMA; QMLKYHI; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047727; F:isobutyryl-CoA mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034784; F:pivalyl-CoA mutase activity; IEA:InterPro.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02050; IcmF; 1.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR033669; IcmF.
DR   InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   PANTHER; PTHR43087:SF1; LAO/AO TRANSPORT SYSTEM ATPASE; 1.
DR   PANTHER; PTHR43087; LYSINE/ARGININE/ORNITHINE TRANSPORT SYSTEM KINASE; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF03308; MeaB; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_02050};
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|HAMAP-Rule:MF_02050};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_02050};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_02050};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02050};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02050};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02050};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02050};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_02050};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02050}.
FT   DOMAIN          11..149
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   BINDING         24
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         210..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         255
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         347..350
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         578
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         613
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         719
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         763
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         812
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         847
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         852
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         964
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         1085
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ   SEQUENCE   1086 AA;  122412 MW;  288EEA7C98CB05C0 CRC64;
     MMAHIYRPKH HVRFVTASSL FDGHDASINI MRRILQASGA EVIHLGHNRS VEEIVNAAIQ
     EDVQGIAVSS YQGGHMEFFK YMYDLLQERG APHIRIYGGG GGVIIPREIK ELHEYGIARI
     FSPEDGRRLG LQGMINVMLE ECDFPTVTAV TDEIERLQTG DVQAIARLIT LCEYRTEAGQ
     EAAAAAEAAI EQVKTMEKRV PVLGITGTGG AGKSSLTDEL VRRFLNEIPE IKIAILSVDP
     TKQKTGGALL GDRIRMNAIH SPRVYMRSLA TRHSRSELSP AIRDAISVVK AAGFDLIIVE
     TSGIGQGDAA ITEVCDVSMY VMTSEFGAPT QLEKIDMIDY ADLIAINKFE RKGSEDAKRQ
     VQKQYQRSRQ LFDRDVSEMP VYGTIASQFN DPGTNTLFVA LVDTINRKTG TNWKTSLNTV
     ANVEKHNVII PNERRYYLRE IAETVRSYHR RAEQQVEIAR RLFQIEGAIE AANERGESDD
     VIRALETLKA DYEAKLTPES KRILATWEET KAKYAAKQLV TKVRDKEIVT ELTTKTLSGL
     DIPKVILPKF KDYGEILRWV YKENVPGSFP YTAGVFPFKR QGEDPKRQFA GEGTPERTNR
     RFHYLCKEDK AKRLSTAFDS VTLYGEDPDY RPDIFGKVGE SGVSICTLDD MKKLYKGFDL
     CDPLTSVSMT INGPAPILLA MFMNTAIDQQ VEKREQELGR PLTAEEYEQV KAATLQTVRG
     TVQADILKED QGQNTCIFST DFALKMMGDI QEYFIKHRVR NYYSVSISGY HIAEAGANPI
     TQLAFTLANG FTYVEYYLSR GMHIDDFAPN LSFFFSNGLD PEYSVIGRVA RRIWAVVMRE
     KYGANERSQK LKYHIQTSGR SLHAQEIDFN DIRTTLQALL AIYDNCNSLH TNAYDEAITT
     PTEESVRRAM AIQLIITKEF GLAKNENPLQ GSFIIEELTD LVEEAVLQEF ERLNDRGGVL
     GAMEMQYQRG KIQDESLYYE TKKHSGELPI IGVNTFLNPN PPSEDELNNL ELARATYEEK
     ELQIRNLREF QERNKDKVGP ALERLKQVAI SGGNIFEELM ETVKVASLGQ ITRALYEVGG
     QYRRNM
//
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